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Originally published In Press as doi:10.1074/jbc.M210951200 on December 16, 2002

J. Biol. Chem., Vol. 278, Issue 8, 5854-5863, February 21, 2003
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The Auto-inhibitory Function of Importin alpha  Is Essential in Vivo*

Michelle T. HarremanDagger §, Mary R. Hodel§, Patrizia Fanara§, Alec E. Hodel§, and Anita H. Corbett§

From the § Department of Biochemistry, School of Medicine and the Dagger  Graduate Program in Biochemistry, Cell and Developmental Biology, Emory University, Atlanta, Georgia 30322

Proteins that contain a classical nuclear localization signal (NLS) are recognized in the cytoplasm by a heterodimeric import receptor composed of importin/karyopherin alpha  and beta . The importin alpha  subunit recognizes classical NLS sequences, and the importin beta  subunit directs the complex to the nuclear pore. Recent work shows that the N-terminal importin beta  binding (IBB) domain of importin alpha  regulates NLS-cargo binding in the absence of importin beta  in vitro. To analyze the in vivo functions of the IBB domain, we created a series of mutants in the Saccharomyces cerevisiae importin alpha  protein. These mutants dissect the two functions of the N-terminal IBB domain, importin beta  binding and auto-inhibition. One of these importin alpha  mutations, A3, decreases auto-inhibitory function without impacting binding to importin beta  or the importin alpha  export receptor, Cse1p. We used this mutant to show that the auto-inhibitory function is essential in vivo and to provide evidence that this auto-inhibitory-defective importin alpha  remains bound to NLS-cargo within the nucleus. We propose a model where the auto-inhibitory activity of importin alpha  is required for NLS-cargo release and the subsequent Cse1p-dependent recycling of importin alpha  to the cytoplasm.

* This work was supported by National Institutes of Health Grant GM-58728 (to A. H. C.) and by National Science Foundation Grant MCB-9874548 (to A. E. H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Biochemistry, School of Medicine, Emory University, 1510 Clifton Rd., NE, Atlanta, GA 30322. Tel.: 404-727-4546; Fax: 404-727-3954; E-mail: acorbe2@emory.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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